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• W4385971844 abstract "Abundant formation of endogenous supersulfides, which include reactive persulfide species and sulfur catenated residues in thiols and proteins (supersulfidation), has been observed. We found here that supersulfides catalyze S-nitrosoglutathione (GSNO) metabolism via glutathione-dependent electron transfer from aldehydes by exploiting alcohol dehydrogenase 5 (ADH5). ADH5 is a highly conserved bifunctional enzyme serving as GSNO reductase (GSNOR) that down-regulates NO signaling and formaldehyde dehydrogenase (FDH) that detoxifies formaldehyde in the form of glutathione hemithioacetal. C174S mutation significantly reduced the supersulfidation of ADH5 and almost abolished GSNOR activity but spared FDH activity. Notably, Adh5C174S/C174S mice manifested improved cardiac functions possibly because of GSNOR elimination and consequent increased NO bioavailability. Therefore, we successfully separated dual functions (GSNOR and FDH) of ADH5 (mediated by the supersulfide catalysis) through the biochemical analysis for supersulfides in vitro and characterizing in vivo phenotypes of the GSNOR-deficient organisms that we established herein. Supersulfides in ADH5 thus constitute a substantial catalytic center for GSNO metabolism mediating electron transfer from aldehydes." @default.
• W4385971844 created "2023-08-19" @default.
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• W4385971844 date "2023-08-18" @default.
• W4385971844 modified "2023-10-06" @default.
• W4385971844 title "Supersulfide catalysis for nitric oxide and aldehyde metabolism" @default.
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• W4385971844 doi "https://doi.org/10.1126/sciadv.adg8631" @default.
• W4385971844 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37595031" @default.
• W4385971844 hasPublicationYear "2023" @default.
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